{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,7,6]],"date-time":"2024-07-06T06:35:56Z","timestamp":1720247756425},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1990,8,1]]},"abstract":"<jats:p>The metabolism of atrial natriuretic peptide (ANP) and Cys-105-Phe-106-cleaved ANP (ANP) was studied during constant infusion of 125I-labelled peptides in rats. Analysis of circulating radioactivity indicated rapid clearance of ANP and ANP\u2032, with mean half-lives of 0.42 and 1.04 min respectively. H.p.l.c. fractionation of plasma taken during the infusion of labelled ANP revealed the presence of three radioactive fragments, the major one co-eluting with 125I-ANP\u2032. These fragments correspond to cleavage products previously found to be generated in vitro by the action of endopeptidase 24.11 (E-24.11). On evaluating the effects of peptidase inhibitors, a significant increase in the half-life of ANP was observed with phosphoramidon (t1\/2 7.8 min) and aprotinin (t1\/2 5.4 min). A maximal inhibition of ANP degradation was obtained when both inhibitors were given simultaneously (t1\/2 15 min). In blood samples taken during infusion of 125I-ANP and phosphoramidon, the intact peptide accounted for more than 90% of total circulating radioactivity, and no cleavage product was present in detectable amounts. Phosphoramidon had no effect on the metabolism of infused ANP\u2032. In contrast, when 125I-ANP\u2032 was infused together with aprotinin, the rate of degradation of the infused peptide was reduced by more than 80%. It is proposed that two different peptidase activities, E-24.11 and a kallikrein-like proteinase, are responsible for the cleavage of ANP in the circulation. The Cys-Phe-cleaved ANP would in turn be degraded by kallikrein and not by E-24.11.<\/jats:p>","DOI":"10.1042\/bj2690801","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:17:14Z","timestamp":1439241434000},"page":"801-806","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Respective roles of kallikrein and endopeptidase 24.11 in the metabolic pathway of atrial natriuretic peptide in the rat"],"prefix":"10.1042","volume":"269","author":[{"given":"Y","family":"Vanneste","sequence":"first","affiliation":[{"name":"Laboratoire Pluridisciplinaire de Recherche Exp\u00e9rimentale Biom\u00e9dicale, Facult\u00e9 de M\u00e9decine, Campus Erasme, Universit\u00e9 Libre de Bruxelles, Brussels, Belgium."}]},{"given":"S","family":"Pauwels","sequence":"additional","affiliation":[{"name":"Department of Nuclear Medicine, University of Louvain Medical School, Brussels, Belgium"}]},{"given":"L","family":"Lambotte","sequence":"additional","affiliation":[{"name":"Laboratory of Experimental Surgery, University of Louvain Medical School, Brussels, Belgium"}]},{"given":"A","family":"Michel","sequence":"additional","affiliation":[{"name":"Laboratoire de Chimie Biologique, Universite de l'Etat, Mons, Belgium"}]},{"given":"R","family":"Dimaline","sequence":"additional","affiliation":[{"name":"Medical Research Council Secretory Control Group, Physiological Laboratory, University of Liverpool, Liverpool L69 3BX, U.K."}]},{"given":"M","family":"Deschodt-Lanckman","sequence":"additional","affiliation":[{"name":"Laboratoire Pluridisciplinaire de Recherche Exp\u00e9rimentale Biom\u00e9dicale, Facult\u00e9 de M\u00e9decine, Campus Erasme, Universit\u00e9 Libre de Bruxelles, Brussels, Belgium."}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/269\/3\/801\/599252\/bj2690801.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/269\/3\/801\/599252\/bj2690801.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T18:36:17Z","timestamp":1637865377000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/269\/3\/801\/26268\/Respective-roles-of-kallikrein-and-endopeptidase"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1990,8,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1990,8,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2690801","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1990,8,1]]}}}